Crystallization and preliminary X-ray diffraction analysis of a novel β-<scp>L</scp>-arabinofuranosidase (HypBA1) fromBifidobacterium longum

The β-L-arabinofuranosidase (HypBA1) fromBifidobacterium longumJCM 1217 hydrolyzes the β-1,2-linked arabinofuranose disaccharide to release L-arabinoses. HypBA1 was classified into glycoside hydrolase family 127 (GH127) by the CAZy website (http://www.cazy.org/). The enzyme was expressed inEscherichia coliand the purified recombinant protein was crystallized. Crystals belonging to the primitive hexagonal space groupP3x21, with unit-cell parametersa=b= 75.9,c= 254.0 &#197;, were obtained by the sitting-drop vapour-diffusion method and diffracted to 2.78 &#197; resolution. ABLASTPsearch (http://blast.ncbi.nlm.nih.gov/) of the Protein Data Bank did not reveal any similar crystal structures. Structural determination by using SeMet MAD and MIR methods is in progress.